CAP_DICDI
ID CAP_DICDI Reviewed; 464 AA.
AC P54654; Q54IG5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Adenylyl cyclase-associated protein;
DE Short=CAP;
GN Name=cap; ORFNames=DDB_G0288769;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX3;
RX PubMed=8688557; DOI=10.1091/mbc.7.2.261;
RA Gottwald U., Brokamp R., Karakesisoglou I., Schleicher M., Noegel A.A.;
RT "Identification of a cyclase-associated protein (CAP) homologue in
RT Dictyostelium discoideum and characterization of its interaction with
RT actin.";
RL Mol. Biol. Cell 7:261-272(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 51-226.
RX PubMed=12962635; DOI=10.1016/s0969-2126(03)00180-1;
RA Ksiazek D., Brandstetter H., Israel L., Bourenkov G.P., Katchalova G.,
RA Janssen K.P., Bartunik H.D., Noegel A.A., Schleicher M., Holak T.A.;
RT "Structure of the N-terminal domain of the adenylyl cyclase-associated
RT protein (CAP) from Dictyostelium discoideum.";
RL Structure 11:1171-1178(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 42-227.
RX PubMed=15558566; DOI=10.1002/prot.20314;
RA Yusof A.M., Hu N.J., Wlodawer A., Hofmann A.;
RT "Structural evidence for variable oligomerization of the N-terminal domain
RT of cyclase-associated protein (CAP).";
RL Proteins 58:255-262(2005).
CC -!- FUNCTION: May have a regulatory bifunctional role. Binds G-actin and
CC PIP2. Involved in microfilament reorganization near the plasma membrane
CC in a PIP2-regulated manner.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- DOMAIN: The C-terminus is responsible for sequestering G-actin. The N-
CC terminus is required for the PIP2 modulation of cap function.
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
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DR EMBL; U43027; AAB09713.1; -; mRNA.
DR EMBL; AAFI02000125; EAL63006.1; -; Genomic_DNA.
DR RefSeq; XP_636512.1; XM_631420.1.
DR PDB; 1S0P; X-ray; 1.40 A; A/B=51-226.
DR PDB; 1TJF; X-ray; 2.21 A; A/B=42-227.
DR PDBsum; 1S0P; -.
DR PDBsum; 1TJF; -.
DR AlphaFoldDB; P54654; -.
DR BMRB; P54654; -.
DR SMR; P54654; -.
DR STRING; 44689.DDB0191139; -.
DR PaxDb; P54654; -.
DR EnsemblProtists; EAL63006; EAL63006; DDB_G0288769.
DR GeneID; 8626797; -.
DR KEGG; ddi:DDB_G0288769; -.
DR dictyBase; DDB_G0288769; cap.
DR eggNOG; KOG2675; Eukaryota.
DR HOGENOM; CLU_015780_1_0_1; -.
DR InParanoid; P54654; -.
DR OMA; LDGNKWI; -.
DR PhylomeDB; P54654; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR EvolutionaryTrace; P54654; -.
DR PRO; PR:P54654; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0044354; C:macropinosome; IDA:dictyBase.
DR GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IDA:dictyBase.
DR GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR GO; GO:0005774; C:vacuolar membrane; IDA:dictyBase.
DR GO; GO:0031982; C:vesicle; IDA:dictyBase.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0008179; F:adenylate cyclase binding; IBA:GO_Central.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IGI:dictyBase.
DR GO; GO:0019933; P:cAMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IGI:dictyBase.
DR GO; GO:0033298; P:contractile vacuole organization; IMP:dictyBase.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IGI:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0006907; P:pinocytosis; IMP:dictyBase.
DR GO; GO:0045761; P:regulation of adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IGI:dictyBase.
DR GO; GO:0006970; P:response to osmotic stress; IMP:dictyBase.
DR Gene3D; 1.25.40.330; -; 1.
DR Gene3D; 2.160.20.70; -; 1.
DR InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
DR InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
DR InterPro; IPR013992; Adenylate_cyclase-assoc_CAP_N.
DR InterPro; IPR017901; C-CAP_CF_C-like.
DR InterPro; IPR016098; CAP/MinC_C.
DR InterPro; IPR036223; CAP_C_sf.
DR InterPro; IPR028417; CAP_CS_C.
DR InterPro; IPR018106; CAP_CS_N.
DR InterPro; IPR036222; CAP_N_sf.
DR InterPro; IPR006599; CARP_motif.
DR PANTHER; PTHR10652; PTHR10652; 1.
DR Pfam; PF08603; CAP_C; 1.
DR Pfam; PF01213; CAP_N; 1.
DR SMART; SM00673; CARP; 2.
DR SUPFAM; SSF101278; SSF101278; 1.
DR SUPFAM; SSF69340; SSF69340; 1.
DR PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
DR PROSITE; PS01088; CAP_1; 1.
DR PROSITE; PS01089; CAP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cell membrane; Membrane; Reference proteome.
FT CHAIN 1..464
FT /note="Adenylyl cyclase-associated protein"
FT /id="PRO_0000205704"
FT DOMAIN 304..443
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT REGION 215..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 52..73
FT /evidence="ECO:0007829|PDB:1S0P"
FT HELIX 75..100
FT /evidence="ECO:0007829|PDB:1S0P"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:1S0P"
FT HELIX 114..128
FT /evidence="ECO:0007829|PDB:1S0P"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:1TJF"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:1S0P"
FT HELIX 146..153
FT /evidence="ECO:0007829|PDB:1S0P"
FT HELIX 158..180
FT /evidence="ECO:0007829|PDB:1S0P"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:1S0P"
FT HELIX 185..208
FT /evidence="ECO:0007829|PDB:1S0P"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:1S0P"
SQ SEQUENCE 464 AA; 49641 MW; 7ABDD05D8A0148B4 CRC64;
MSEATIVELL KRLDQATTRL EAVEKSIASG VASSSSSSSP SSGAAGPSSA SVKEFQNLVD
QHITPFVALS KKLAPEVGNQ VEQLVKAIDA EKALINTASQ SKKPSQETLL ELIKPLNNFA
AEVGKIRDSN RSSKFFNNLS AISESIGFLS WVVVEPTPGP HVAEMRGSAE FYTNRILKEF
KGVNQDQVDW VSNYVNFLKD LEKYIKQYHT TGLTWNPKGG DAKSATPAPA SSAPAAPVAP
AVSSTPVESK KGPGLGAVFG ELSKGDGVTS GLKKVTNDMK SKNFTDKSSV VKAADTKVAK
VDAPSRPAVF ALQGNKWSIE YQVNNKEIVI AEPDSRQTVY IFQCVNSLVQ IKGKVNAITL
DGCKKTSIVF ENAISSCEVV NCNGVEIQVT GRVPSIAIDK TSGCQIYLSK DSLETEIVSS
KSSEMNVLIP GATENDDLVE LAIPEQYKTS VKGNKLHTES TSHI
